Reactions of cytochrome c oxidase with sodium dithionite.
Reactions of cytochrome c oxidase with sodium dithionite.
复制标题
细胞色素c氧化酶与连二亚硫酸钠的反应。
DOI:
10.1042/bj2090175
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发表时间:
1983
期刊:
影响因子:
--
通讯作者:
P. Sarti
中科院分区:
文献类型:
--
作者:
G. Jones;M. G. Jones;M. Wilson;M. Brunori;A. Colosimo;P. Sarti
The reduction of cytochrome c oxidase (EC 1.9.3.1) by dithionite was investigated by stopped-flow spectrophotometry and flow-flash techniques in the presence of CO. Of the two haem groups present in the enzyme, that associated with cytochrome alpha is the first reduced. The second-order rate constants for reduction of a number of redox proteins (cytochrome c, stellacyanin and azurin) by the S2O4(2-) and SO2.- anions are reported, and the values are compared with those determined for cytochrome c oxidase. These results are discussed in terms of the accessibility and charge distribution of the electron-entry site of cytochrome c oxidase.